CAMK2δ is a serine/threonine protein kinase that is a member of the type II multifunctional Ca2+/calmodulin-dependent protein kinase family. CAMK2δ is abundantly present in human cardiac and skeletal muscle and its levels are increased in the heart of patients suffering from cardiomyopathy. In cardiomyocytes, stimulation of beta-1-adrenergic receptor leads to induction of apoptosis, an effect that is mediated by activation of CAMK2δ in a PKA-independent manner. In addition, expression studies have revealed the downregulation of CAMK2δ in human tumor cells.
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The Journal of clinical investigation, 111(5), 617-625 (2003-03-06)
beta(1)-adrenergic receptor (beta(1)AR) stimulation activates the classic cAMP/protein kinase A (PKA) pathway to regulate vital cellular processes from the change of gene expression to the control of metabolism, muscle contraction, and cell apoptosis. Here we show that sustained beta(1)AR stimulation
Despite its importance for the regulation of heart function, little is known about the isoform expression of the multifunctional Ca2+/calmodulin-dependent protein kinase (CaMKII) in human myocardium. In this study, we investigated the spectrum of CaMKII isoforms delta2, delta3, delta4, delta8
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